2f1s
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2f1s.gif|left|200px]] | [[Image:2f1s.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2f1s", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | | | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | + | --> | |
| - | + | {{STRUCTURE_2f1s| PDB=2f1s | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''Crystal Structure of a Viral FLIP MC159''' | '''Crystal Structure of a Viral FLIP MC159''' | ||
| Line 29: | Line 26: | ||
[[Category: Shi, Y.]] | [[Category: Shi, Y.]] | ||
[[Category: Yu, J W.]] | [[Category: Yu, J W.]] | ||
| - | [[Category: | + | [[Category: Caspase activation]] |
| - | [[Category: | + | [[Category: Death receptor signaling]] |
| - | [[Category: | + | [[Category: Ded]] |
| - | [[Category: | + | [[Category: Disc]] |
| - | [[Category: | + | [[Category: Flip]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:21:47 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 00:21, 4 May 2008
Crystal Structure of a Viral FLIP MC159
Overview
Death receptor signaling is initiated by the assembly of the death-inducing signaling complex, which culminates in the activation of the initiator caspase, either caspase-8 or caspase-10. A family of viral and cellular proteins, known as FLIP, plays an essential role in the regulation of death receptor signaling. Viral FLIP (v-FLIP) and short cellular FLIP (c-FLIPS) inhibit apoptosis by interfering with death receptor signaling. The structure and mechanisms of v-FLIP and c-FLIPS remain largely unknown. Here we report a high resolution crystal structure of MC159, a v-FLIP derived from the molluscum contagiosum virus, which is a member of the human poxvirus family. Unexpectedly, the two tandem death effector domains (DEDs) of MC159 rigidly associate with each other through a hydrophobic interface. Structure-based sequence analysis suggests that this interface is conserved in the tandem DEDs from other v-FLIP, c-FLIPS, and caspase-8 and -10. Strikingly, the overall packing arrangement between the two DEDs of MC159 resembles that between the caspase recruitment domains of Apaf-1 and caspase-9. In addition, each DED of MC159 contains a highly conserved binding motif on the surface, to which loss-of-function mutations in MC159 map. These observations, in conjunction with published evidence, reveal significant insights into the function of v-FLIP and suggest a mechanism by which v-FLIP and c-FLIPS inhibit death receptor signaling.
About this Structure
2F1S is a Single protein structure of sequence from Molluscum contagiosum virus subtype 1. Full crystallographic information is available from OCA.
Reference
Crystal structure of a viral FLIP: insights into FLIP-mediated inhibition of death receptor signaling., Li FY, Jeffrey PD, Yu JW, Shi Y, J Biol Chem. 2006 Feb 3;281(5):2960-8. Epub 2005 Nov 29. PMID:16317000 Page seeded by OCA on Sun May 4 03:21:47 2008
